ID G9ZE81_9GAMM Unreviewed; 756 AA.
AC G9ZE81;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Ribonuclease R {ECO:0000256|HAMAP-Rule:MF_01895};
DE Short=RNase R {ECO:0000256|HAMAP-Rule:MF_01895};
DE EC=3.1.13.1 {ECO:0000256|HAMAP-Rule:MF_01895};
GN Name=rnr {ECO:0000256|HAMAP-Rule:MF_01895};
GN ORFNames=HMPREF9080_01066 {ECO:0000313|EMBL:EHM54955.1};
OS Cardiobacterium valvarum F0432.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC Cardiobacteriaceae; Cardiobacterium.
OX NCBI_TaxID=797473 {ECO:0000313|EMBL:EHM54955.1, ECO:0000313|Proteomes:UP000004750};
RN [1] {ECO:0000313|EMBL:EHM54955.1, ECO:0000313|Proteomes:UP000004750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0432 {ECO:0000313|EMBL:EHM54955.1,
RC ECO:0000313|Proteomes:UP000004750};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside
CC monophosphates and is involved in maturation of structured RNAs.
CC {ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.13.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001849, ECO:0000256|HAMAP-
CC Rule:MF_01895};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHM54955.1}.
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DR EMBL; AGCM01000054; EHM54955.1; -; Genomic_DNA.
DR AlphaFoldDB; G9ZE81; -.
DR STRING; 797473.HMPREF9080_01066; -.
DR PATRIC; fig|797473.3.peg.866; -.
DR HOGENOM; CLU_002333_7_0_6; -.
DR Proteomes; UP000004750; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016070; P:RNA metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd04471; S1_RNase_R; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR004476; RNase_II/RNase_R.
DR InterPro; IPR011805; RNase_R.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR00358; 3_prime_RNase; 1.
DR NCBIfam; TIGR02063; RNase_R; 1.
DR PANTHER; PTHR23355:SF9; DIS3-LIKE EXONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 1.
DR Pfam; PF17876; CSD2; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01895};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01895};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01895};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 523..604
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 611..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 756 AA; 83337 MW; A1515AFF1D4CC3D3 CRC64;
MAELMHGDKI LARVKHEDDS GRKDYAPVEI LERAQKRIVG KLAVQHGVWT LVPENRRLTQ
HMLIPAGELG GGKAGQVVIG EITAYPSRYR QPIGKIIAVL GEAMSAGMET DIAIENHNIP
AEFPADVLAE SASLPDELQA EDYDNRLDLR HLPFVTIDGI TARDFDDAVY AEKRGSNYRL
YVAIADVAHY VRPDSPLDAE AYNRGTSVYF PDRVIPMLPE KLSNGLCSLN PDVDRLAMVC
EITLAPDGSI KRSAFHDAVI HSHARLTYET VEEILFADNT LLRDSFARLA RPLDTLKSVY
HILHAAREAR SVIDFHAAEP EFIYDSEGKI ETIKTRERLE SHRLIEECMI AANICAAKTI
GKHKIPALYR VHDDPSEERL ARLIDFLGKR GIRWQGGAES ATPQQFSELL SRCAERPDYA
QIETMVLRSM SQAIYVPDNR GHFGLALEHY AHFTSPIRRY PDLLVHRAIR HHLHGGSRED
YPYSAESMVE KGKHCSMTER RADEATRDAM DFLKCEFMSH RIGEHYHGRI AGITNFGFFV
ALDDLGIDGL VHVSTLTNDY YHYHSDTFTL TGERSGYRFA LMDEVEIQVA KVDLEDRKID
FELIAHQGKA LGGGKKRGKT TAPPAQTTTP AAKTTEPAQV TKTAKAAKTT KTAEKATKPA
KVEKAAKTAG KTAKPAAAKA AKTAEKAAKS AKTTKAAKTA EKAAKPAKTA KAAKTAEKAA
KPAKAAKATK TAAKTAKTEK AAKKTAAKAK RTKKNA
//
